Projects per year
Abstract / Description of output
Mis18 is a key regulator responsible for the centromere localization of the CENP-A chaperone Scm3 in S. pombe and HJURP in humans, which establishes CENP-A chromatin that defines centromeres. The molecular and structural determinants of Mis18 centromere targeting remain elusive. Here, by combining structural, biochemical and yeast genetic studies, we show that the oligomerization of S. pombe Mis18, mediated via its conserved N-terminal Yippee-like domain, is crucial for its centromere localization and function. The crystal structure of the N-terminal Yippeelike domain reveals a fold containing a cradle-shaped pocket that is implicated in protein/nucleic acid binding, which we show is required for Mis18 function. While the N-terminal Yippee-like domain forms a homodimer in vitro and in vivo, full length Mis18, including the C-terminal α-helical domain, forms a homotetramer in vitro. We also show that the Yippee-like domains of human Mis18α/Mis18β interact to form a heterodimer, implying a conserved structural theme for Mis18 regulation.
Original language | English |
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Journal | EMBO Reports |
Early online date | 26 Feb 2016 |
DOIs | |
Publication status | E-pub ahead of print - 26 Feb 2016 |
Keywords / Materials (for Non-textual outputs)
- CENP-A
- Centromere
- Epigenetics
- Mis18
- Yippee
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Dive into the research topics of 'Centromere Localization and Function of Mis18 Requires 'Yippee-like' Domain-Mediated Oligomerization: Crystal Structure of Mis18 ‘Yippee-like’ Domain'. Together they form a unique fingerprint.Projects
- 7 Finished
Profiles
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Robin Allshire
- School of Biological Sciences - Professor of Chromosome Biology
- Centre for Engineering Biology
Person: Academic: Research Active
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Jeyaprakash Arulanandam
- School of Biological Sciences - Personal Chair of Structural Cell Biology
Person: Academic: Research Active